2otb
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(New page: 200px<br /><applet load="2otb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2otb, resolution 1.790Å" /> '''Crystal structure o...)
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Revision as of 11:10, 21 November 2007
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Crystal structure of a monomeric cyan fluorescent protein in the fluorescent state
Overview
Fluorescent protein (FP) variants that can be reversibly converted between, fluorescent and nonfluorescent states have proven to be a catalyst for, innovation in the field of fluorescence microscopy. However, the, structural basis of the process remains poorly understood. High-resolution, structures of a FP derived from Clavularia in both the fluorescent and the, light-induced nonfluorescent states reveal that the rapid and complete, loss of fluorescence observed upon illumination with 450-nm light results, from cis-trans isomerization of the chromophore. The photoinduced change, in configuration from the well ordered cis isomer to the highly nonplanar, and disordered trans isomer is accompanied by a dramatic rearrangement of, internal side chains. Taken together, the structures provide an, explanation for the loss of fluorescence upon illumination, the slow, light-independent recovery, and the rapid light-induced recovery of, fluorescence. The fundamental mechanism appears to be common to all of the, photoactivatable and reversibly photoswitchable FPs reported to date.
About this Structure
2OTB is a Single protein structure of sequence from Clavularia sp.. Full crystallographic information is available from OCA.
Reference
Structural basis for reversible photobleaching of a green fluorescent protein homologue., Henderson JN, Ai HW, Campbell RE, Remington SJ, Proc Natl Acad Sci U S A. 2007 Apr 17;104(16):6672-7. Epub 2007 Apr 9. PMID:17420458
Page seeded by OCA on Wed Nov 21 13:17:35 2007
